Identification of a calcium- and phospholipid-dependent protein kinase in plant tissue

A Ca 2+- and phospholipid-activated protein kinase from zucchini has been partially purified by DEAE-Sephacel chromatography and some properties of the enzyme have been assessed. Minimal activity occurs in the absence of added Ca 2+ or of added phospholipid but concentrations of the free ion in the...

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Bibliographic Details
Published in:FEBS letters 1985-07, Vol.187 (1), p.25-28
Main Authors: Schäfer, Angelika, Bygrave, Fyfe, Matzenauer, Sybille, Marmé, Dieter
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Protein kinase Calcium Phospholipid Protein phosphorylation Plant
Protein kinaseCalciumPhospholipidProtein phosphorylationPlant
Transferases
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Summary:A Ca 2+- and phospholipid-activated protein kinase from zucchini has been partially purified by DEAE-Sephacel chromatography and some properties of the enzyme have been assessed. Minimal activity occurs in the absence of added Ca 2+ or of added phospholipid but concentrations of the free ion in the range of 3 × 10 −7 M produce a marked stimulation. At 10 −6 M free Ca 2+ this activity is further enhanced by phosphatidylserine, phosphatidylethanolamine and phosphatidic acid but not by phosphatidylcholine or phosphatidylinositol. All of these phospholipids and especially phosphatidylinositol stimulate protein kinase activity in the absence of added Ca 2+.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)81206-0